Zinc in PDB 3wrn: Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication

The structure of Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication, PDB code: 3wrn was solved by S.K.Tewary, H.Zhao, L.Tang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.33 / 1.52
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	56.790, 121.430, 41.560, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 19.9

The structure of Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Zinc atom in the Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication (pdb code 3wrn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication, PDB code: 3wrn:

Zinc binding site 1 out of 1 in the Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Minute Virus of Mice Non-Structural Protein-1N-Terminal Nuclease Domain Reveals A Unique ZN2+ Coordination in the Active Site Pocket and Shows A Novel Mode of Dna Recognition at the Origin of Replication within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:16.7 occ:0.53 O A:HOH549 1.9 29.3 1.0 OE1 A:GLU119 2.0 24.3 1.0 NE2 A:HIS129 2.1 21.1 1.0 NE2 A:HIS127 2.1 19.7 1.0 O A:HOH434 2.3 26.3 1.0 O A:HOH553 2.9 32.3 1.0 CD2 A:HIS129 3.0 21.2 1.0 CD2 A:HIS127 3.1 18.8 1.0 CE1 A:HIS127 3.1 18.5 1.0 CE1 A:HIS129 3.1 21.2 1.0 CD A:GLU119 3.2 14.6 0.6 CB A:GLU119 3.8 18.0 1.0 CG A:GLU119 4.0 19.5 1.0 O A:HOH528 4.1 41.4 1.0 OE2 A:GLU119 4.1 21.1 1.0 O A:HOH533 4.1 42.1 1.0 CG A:HIS129 4.2 18.5 1.0 ND1 A:HIS127 4.2 16.2 1.0 ND1 A:HIS129 4.2 19.7 1.0 O A:HOH458 4.2 32.8 1.0 CG A:HIS127 4.2 16.4 1.0 NZ A:LYS214 4.3 23.1 1.0

S.K.Tewary, L.Liang, Z.Lin, A.Lynn, S.F.Cotmore, P.Tattersall, H.Zhao, L.Tang. Structures of Minute Virus of Mice Replication Initiator Protein N-Terminal Domain: Insights Into Dna Nicking and Origin Binding. Virology V.476C 61 2014.
ISSN: ISSN 0042-6822
PubMed: 25528417
DOI: 10.1016/J.VIROL.2014.11.022